Catalytic mechanisms and biocatalytic applications of aspartate and methylaspartate ammonia lyases.

Abstract:

:Ammonia lyases catalyze the formation of α,β-unsaturated bonds by the elimination of ammonia from their substrates. This conceptually straightforward reaction has been the emphasis of many studies, with the main focus on the catalytic mechanism of these enzymes and/or the use of these enzymes as catalysts for the synthesis of enantiomerically pure α-amino acids. In this Review aspartate ammonia lyase and 3-methylaspartate ammonia lyase, which represent two different enzyme superfamilies, are discussed in detail. In the past few years, the three-dimensional structures of these lyases in complex with their natural substrates have revealed the details of two elegant catalytic strategies. These strategies exploit similar deamination mechanisms that involve general-base catalyzed formation of an enzyme-stabilized enolate anion (aci-carboxylate) intermediate. Recent progress in the engineering and application of these enzymes to prepare enantiopure l-aspartic acid derivatives, which are highly valuable as tools for biological research and as chiral building blocks for pharmaceuticals and food additives, is also discussed.

journal_name

ACS Chem Biol

journal_title

ACS chemical biology

authors

de Villiers M,Puthan Veetil V,Raj H,de Villiers J,Poelarends GJ

doi

10.1021/cb3002792

subject

Has Abstract

pub_date

2012-10-19 00:00:00

pages

1618-28

issue

10

eissn

1554-8929

issn

1554-8937

journal_volume

7

pub_type

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